9js5
From Proteopedia
Crystal structure of the ASFV-derived histone-like protein pA104R
Structural highlights
FunctionPublication Abstract from PubMedAfrican swine fever is a highly lethal disease caused by the African swine fever virus (ASFV), posing a significant threat to the global pig industry, wherease no approved treatments are currently available. The ASFV DNA-binding protein, pA104R, plays a critical role in viral genome packaging and replication, making it a key target for drug discovery. Through structure-based virtual screening, we identified a polyphenolic compound, thonningianin A, which disrupts the pA104R-DNA binding and significantly inhibits ASFV replication. Mechanistic study revealed that thonningianin A binds to the DNA-binding region of pA104R, forming strong hydrogen bonds with H100 and occupying the vital DNA-binding residues K92, R94, and K97. In addition, we resolved the high-resolution (1.8 A) structure of pA104R (PDB ID 9JS5), providing valuable insights for future drug screening. Together, these results demonstrate that thonningianin A holds great potential for the development of anti-ASFV drug, as a herb extract with favourable pharmacokinetic properties and safety. Thonningianin A disrupts pA104R-DNA binding and inhibits African swine fever virus replication.,Li QJ, Shao HH, Zheng LL, Liu Q, Huo CC, Yi DR, Feng T, Cen S Emerg Microbes Infect. 2025 Dec;14(1):2482697. doi: , 10.1080/22221751.2025.2482697. Epub 2025 Apr 1. PMID:40138179[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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